SARA CANTONE¹*, PATRIZIA SPIZZO¹, DIANA FATTOR¹, VALERIO FERRARIO², CYNTHIA EBERT², LUCIA GARDOSSI^1,2
*Corresponding author
1. SPRIN S.p.A., Technologies for Sustainable Chemistry, via Flavia 23/1, Trieste, 34148, Italy
2. Università degli Studi di Trieste, Dipartimento di Scienze Chimiche e Farmaceutiche, Piazzale Europa 1, Trieste, 34127, Italy

Abstract

Lipases have a wide industrial impact in the food, pharma and cosmetic sectors but there is an enormous catalytic potential waiting to be exploited for biomass transformations. In order to make biotransformations competitive for such bulk production, efficient biocatalysts at affordable costs are needed. Nowadays, the scientific knowledge on lipases structural and functional properties are so advanced that tailored solutions can be provided for formulating and immobilising lipases for specific applications. This objective can be achieved also with the contribution of computational and statistical methods that are able to manage the amazing complexity of the systems under study. However, this knowledge will translate into new and more efficient industrial biocatalysts only if firms have easier access to a wider array of fermented lipases, which must be also amenable to be immobilised under reproducible conditions. These biocatalysts will help to fill the gap between highly optimised “classical” chemical processes and innovative biotransformations.

LIPASES: UNUSUAL HYDROLASES WITH ENORMOUS CATALYTIC POTENTIAL

Lipases are of enormous practical importance for the food, pharma and cosmetic industry (1). Moreover, their applicability in the biofuel and material sectors is under study. Scientific achievements at lab scale should now be transferred to the industrial scale thanks to appropriate solutions and technological integration (2, 3).
Lipases are enzymes that in nature catalyse the hydrolysis of ester bonds of triacylglycerols producing glycerol and fatty acids (triacylglycerol hydrolases EC 3.1.1.3). Their popularity in industrial biotransformation is motivated by their activity and stability in hydrophobic organic solvents at low water activity, so that, they can be efficiently used in different organic media or on bulk hydrophobic substrates (1). This is not surprising considering that the physiological environment of lipases is far from being a diluted aqueous solution. Actually these enzymes are often embedded into phospholipid membranes and work at the lipid-water interface on substrates that are not soluble in water. Indeed, catalytic activity of most lipases is enhanced upon contact ...